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Info message

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Dr. Roger Benoit

Kurzbeschreibung
Tenured Scientist, Principal Investigator
Roger Benoit
E-Mail
roger.benoit@psi.ch
Telefon
+41 56 310 47 03
Orc-ID
0000-0001-9420-7739
Paul Scherrer Institut PSI
Forschungsstrasse 111
5232 Villigen PSI
Schweiz
Digitale Visitenkarte
Inhalt

Research

Structure-function relationships of ACE2 across multiple biological scales

The protein angiotensin-converting enzyme 2 (ACE2), a zinc metallopeptidase, plays key roles in physiological processes involved in health and disease. It became widely known as the receptor used by SARS-CoV and SARS-CoV-2 for cell recognition and entry (Zhou et al., 2020, PMID: 32015507). ACE2 is a main node in the protective arm of the renin-angiotensin-aldosterone system (RAAS) of blood pressure control, and is involved in development, inflammation, immunity, and neurodegenerative deseases (PMID: 23686164). ACE-like proteins have also been identified as components in venoms, for example from scorpions or spiders (PMID: 331463). In addition to its peptidase activities, ACE2 is involved in other processes, such as the regulation of interstinal neutral amino acid transport (PMID: 21814048). 

The enzyme is gaining increased attention as a drug target for hypertension, cardiovascular disease, diabetes, and other disorders. ACE2 is present on the cell surface of various tissues with a specific distribution and can be released into solution by sheddases (PMID: 15983030). 

Structurally, the extracellular or soluble part of ACE2 comprises an N-terminal peptidase domain with a wide, deep substate binding cleft flanking the conserved Zinc-ion binding site, followed by a smaller non-catalytic domain (PMID: 14754895). In the full-length protein, the non-catalytic domain domain extends into a single transmembrane helix and an intracellular domain.

ACE2 Structure
ACE2 Structure

My research focuses on the study of the structure, conformation, and biophysics of ACE2 in the context of novel peptides and small molecule inhibitors, and its interactions with the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) glycoprotein. Another important aspect towards a detailed understanding of ACE2 function is its ultrastructure and interactions in a cellular context across different scales, ranging from molecules to cells and tissues. This requires identification of the protein of interest in its natural, crowded environment of cells.  

Beamlines and tools

Exploring the function of ACE2 (or other proteins) across multiple scales requires access to a wide range of specialized equipment, and interdisciplinary collaborations.

Our department is equipped with state-of-the-art light- and electron microscopy facilities, allowing the tracking of proteins in cells. Access to various beamlines is of key importance. The PSI macromolecular crystallography beamlines X06SA (PXI) and X06DA (PXIII) provide bright collimated X-ray beams to study protein structure and interactions with ligands at near-atomic resolution. The beamline X02DA (TOMCAT) has been constructed for X-ray imaging by synchrotron tomographic microscopy, which enables X-ray imaging of larger objects such as whole cells or tissues. The SwissFEL X-ray free electron laser (SwissFEL) generates a very intense and focused beam of X-rays at short pulses, enabling the study time-resolved changes in protein structures. 

Biomolecular Nanoengineering
X06SA beamline
X06DA beamline
X02DA beamline
SwissFEL X-ray free electron laser beamline

Team members

Aristea
Dr. Aristea Anna Leventi
aristea.leventi@psi.ch
+41 56 310 59 30
Zum Personenprofil
Thorsten Phillips
Dr. Torsten Richard Phillips
torsten.phillips@psi.ch
+41 56 310 23 79
Zum Personenprofil

Education

Biochemie und Molekularbiologie - SpringerSpektrum - 2024, 2nd Edition 

Christen - Jaussi - Benoit 

ISBN Softcover 978-3-662-65476-7; ISBN eBook 978-3-662-65477-4
Biochemie und Molekularbiologie
Webpage

Curriculum Vitae
Team pictures

Publications

  • Gupta R, Schärer P, Liao Y, Roy B, Benoit RM, Shivashankar GV
    Regulation of p65 nuclear localization and chromatin states by compressive force
    Molecular Biology of the Cell. 2025; 36(4): 36:ar37 (12 pp.). https://doi.org/10.1091/mbc.E23-11-0431
    DORA PSI
  • Christen P, Jaussi R, Benoit R
    Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
    2nd ed. Berlin: Springer Nature; 2024. https://doi.org/10.1007/978-3-662-65477-4
    DORA PSI
  • Wang J, Beyer D, Vaccarin C, He Y, Tanriver M, Benoit R, et al.
    Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2
    European Journal of Nuclear Medicine and Molecular Imaging. 2024; 52: 9-21. https://doi.org/10.1007/s00259-024-06831-6
    DORA PSI
  • Behbahanipour M, Benoit R, Navarro S, Ventura S
    OligoBinders: bioengineered soluble amyloid-like nanoparticles to bind and neutralize SARS-CoV-2
    ACS Applied Materials and Interfaces. 2023; 15(9): 11444-11457. https://doi.org/10.1021/acsami.2c18305
    DORA PSI
  • Farnung J, Muhar M, Liang JR, Tolmachova KA, Benoit RM, Corn JE, et al.
    Semisynthetic LC3 probes for autophagy pathways reveal a noncanonical LC3 interacting region motif crucial for the enzymatic activity of human ATG3
    ACS Central Science. 2023; 9(5): 1025-1034. https://doi.org/10.1021/acscentsci.3c00009
    DORA PSI
  • Collu G, Bierig T, Krebs A-S, Engilberge S, Varma N, Guixà-González R, et al.
    Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
    Structure. 2022; 30(1): 95-106. https://doi.org/10.1016/j.str.2021.09.002
    DORA PSI
  • Bierig T, Collu G, Blanc A, Poghosyan E, Benoit RM
    Design, expression, purification, and characterization of a YFP-tagged 2019-n CoV spike receptor-binding domain construct
    Frontiers in Bioengineering and Biotechnology. 2020; 8: 618615 (10 pp.). https://doi.org/10.3389/fbioe.2020.618615
    DORA PSI
  • Skopintsev P, Ehrenberg D, Weinert T, James D, Kar RK, Johnson PJM, et al.
    Femtosecond-to-millisecond structural changes in a light-driven sodium pump
    Nature. 2020; 583: 314-318. https://doi.org/10.1038/s41586-020-2307-8
    DORA PSI
  • Krebs A-S, Bierig T, Collu G, Benoit RM
    Seamless insert-plasmid assembly at sub-terminal homologous sequences
    Plasmid. 2019; 106: 102445 (9 pp.). https://doi.org/10.1016/j.plasmid.2019.102445
    DORA PSI
  • Benoit RM
    Botulinum neurotoxin diversity from a gene-centered view
    Toxins. 2018; 10(8): 310 (14 pp.). https://doi.org/10.3390/toxins10080310
    DORA PSI
  • Benoit RM, Schärer MA, Wieser MM, Li X, Frey D, Kammerer RA
    Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C
    Scientific Reports. 2017; 7: 43588 (7 pp.). https://doi.org/10.1038/srep43588
    DORA PSI
  • Heydenreich FM, Miljuš T, Jaussi R, Benoit R, Milić D, Veprintsev DB
    High-throughput mutagenesis using a two-fragment PCR approach
    Scientific Reports. 2017; 7: 6787 (11 pp.). https://doi.org/10.1038/s41598-017-07010-4
    DORA PSI
  • Benoit RM, Ostermeier C, Geiser M, Li JSZ, Widmer H, Auer M
    Seamless insert-plasmid assembly at high efficiency and low cost
    PLoS One. 2016; 11(4): e0153158 (13 pp.). https://doi.org/10.1371/journal.pone.0153158
    DORA PSI
  • Bianchi S, van Riel WE, Kraatz SHW, Olieric N, Frey D, Katrukha EA, et al.
    Structural basis for misregulation of kinesin KIF21A autoinhibition by CFEOM1 disease mutations
    Scientific Reports. 2016; 6: 30668 (16 pp.). https://doi.org/10.1038/srep30668
    DORA PSI
  • Christen P, Jaussi R, Benoit R
    Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
    Berlin, Heidelberg: Springer; 2016. https://doi.org/10.1007/978-3-662-46430-4
    DORA PSI
  • Benoit RM, Frey D, Wieser MM, Thieltges KM, Jaussi R, Capitani G, et al.
    Structure of the BoNT/A1 - Receptor complex
    Toxicon. 2015; 107(Part A): 25-31. https://doi.org/10.1016/j.toxicon.2015.08.002
    DORA PSI
  • Benoit RM, Frey D, Hilbert M, Kevenaar JT, Wieser MM, Stirnimann CU, et al.
    Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
    Nature. 2014; 505(7481): 108-111. https://doi.org/10.1038/nature12732
    DORA PSI
  • Kammerer RA, Benoit RM
    Botulinum neurotoxins: new questions arising from structural biology
    Trends in Biochemical Sciences. 2014; 39(11): 517-526. https://doi.org/10.1016/j.tibs.2014.08.009
    DORA PSI
  • Benoit RM, Meisner N-C, Kallen J, Graff P, Hemmig R, Cèbe R, et al.
    The X-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible hur redox sensing mechanism
    Journal of Molecular Biology. 2010; 397(5): 1231-1244. https://doi.org/10.1016/j.jmb.2010.02.043
    DORA PSI

 

Benoit RM and Auer M 
A direct way of redox sensing 
RNA Biol 2011;8:18-23
DOI: 10.4161/rna.8.1.13555
 


Meisner N.C., Hintersteiner M., Seifert J.M., Bauer R., Benoit R.M., Widmer A., Schindler T., Uhl V., Lang M., Gstach H., Auer M.
Terminal adenosyl transferase activity of posttranscriptional regulator HuR revealed by confocal on-bead screening.
J Mol Biol. 2009; 386: 435-450
DOI: 10.1016/j.jmb.2008.12.020


Benoit, R.M., Wilhelm, R.N., Scherer-Becker, D., Ostermeier, C.
An improved method for fast, robust, and seamless integration of DNA fragments into multiple plasmids.
Protein Expr Purif. 2006; 45: 66-71
DOI: 10.1016/j.pep.2005.09.022

Preprints


Collu G., Mohammed I., Lafita A., Bierig T., Poghosyan E., Bliven S., Benoit R.M. 
Cryo-EM structure of a single-chain β1-adrenoceptor – AmpC β-lactamase fusion protein
bioRxiv. 2021; doi: https://doi.org/10.1101/2021.09.25.461805

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